FOOD CHEMISTRY
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2025
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IF 9.8
Wangli Dai,Shulai Liu,Yanbo Wang,Yuting Ding,Xuxia Zhou
Maintaining the flavor quality of aquatic products during storage is crucial for their market value and consumer acceptance. This study evaluated the effects of a chitosan-epigallocatechin gallate coating on the flavor profile of bighead carp fillets and explored its underlying regulatory mechanisms. Sensory evaluation, electronic nose, and analysis of volatile and ATP-related compounds revealed that the coating significantly reduced off-flavor compounds, improving flavor quality. The coating suppressed free amino acid and free fatty acid levels, inhibited flavor-converting enzyme activities, and slowed lipid metabolism. Correlation analysis highlighted positive links between key flavor compounds and flavor precursors, enzymes, and metabolites. High-throughput sequencing identified Lactococcus , Serratia , and Aeromonas as key microorganisms affecting flavor characteristics. These findings advance the understanding of flavor deterioration mechanisms and suggest potential strategies for preserving the flavor quality of bighead carp fillets during chilled storage.
研究领域:
食品科学
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分子生物学
✓ 已验证
DOI
PubMed
高影响因子
Food Bioscience
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2021
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IF 4.24
Li Yuan,Yunfei Kong,Weijun Leng,Yanmin Wang,Wengang Jin,Ruichang Gao
The myosin aggregation of b.ighead carp ( Aristichthys nobilis ) induced by heating and the physical structure of surimi gels were changed using L-Glu. L-Glu increased the solubility of myosin regardless of heating or low/high ionic strength . Compared to myosin, the hydrophobicity of myosin with L-Glu at low ionic strength increased significantly, however there was no difference between myosin and myosin with L-Glu at high ionic strength. Atomic force microscopy and scanning electron microscopy results showed that L-Glu suppressed myosin aggregation, forming a honeycomb-like network after a two-step heating. Consequently, the suppression by L-Glu of myosin aggregation changed the physical properties of surimi gels. The water holding capacity of surimi gels with L-Glu increased significantly, but the hardness decreased. This study suggested that the influence of myosin aggregation induced using L-Glu increased ion-dipole interactions, hydrogen bonds and electrostatic repulsions, which changed the microstructure of surimi. L-Glu could be used as an additive to soften surimi gels with low salt for those with difficulty in chewing .
研究领域:
食品科学
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生物化学
✓ 已验证
产品关联
DOI
高影响因子
INTERNATIONAL JOURNAL OF FOOD PROPERTIES
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2018
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IF 1.845
Li Yuan,Qingling Dang,Jianlou Mu,Xueping Feng,Ruichang Gao
Water-holding capacity is closely related to gel microstructure, and is a very important quality trait in surimi and surimi product. The changes in the secondary structure, gel microstructure, and the migration of water in bighead carp (Aristichthys nobilis) myosin gel induced by different temperatures (50–90°C) were investigated. The α-helical structure of myosin decreased at temperatures of 40°C or higher. The fractal dimension of the gels increased at 40, 50, and 60°C, but decreased at temperatures over 60°C. The pore size of the gels increased with temperatures up to 50°C, decreased at 60°C, and then increased with temperatures up to 90°C again. The transverse relaxation times also varied; T21 remained constant at temperatures over 40°C; T22 decreased at temperatures lower than 50°C, increased at 60°C, and then decreased with temperatures up to 90°C; and T23 increased at temperatures lower than 50°C and then remained constant until 90°C. Principal component analysis showed that the proportion of T22 water (PT22) was inversely correlated with the unfolding of myosin, whereas directly correlated with the pore size. The proportion of T23 water (PT23) was positively correlated with the fractal dimensions of the gels, whereas negatively correlated with the pore size. The migration of the secondary layer of water was mainly caused by hydrophobic force and the physical space formed by the myosin backbone, and the migration of water within the third layer was mainly caused by capillary pressure. Therefore, the mobility and redistribution of waters depend on the water retention mechanism, which is determined by the physical structure of gels. This study provides further information about the relationship between the NMR data, gel microstructure, water mobility, and distribution.
研究领域:
食品科学
·
生物化学
✓ 已验证
产品关联
DOI
高影响因子
FOOD HYDROCOLLOIDS
·
2024
·
IF 11
Zhongyang Ren,Xianglan Huang,Yongqiang Zhao,Linfan Shi,Shen Yang,Ritian Jin,Rong Lin,Shuji Liu,Zhiyu Liu,Yucang Zhang,Wuyin Weng
Emulsions could be utilized to improve surimi gels. How myosin-kappa carrageenan (κC) Pickering emulsions to affect the quality of bighead carp surimi is still unclear. The particle distribution of myosin-κC Pickering emulsion was characterized as uniform and stable through particle size potential and microstructure observations. The impact of oil substitution rate on the gel quality of bighead carp ( Aristichthys nobilis ) surimi was investigated by incorporating substitution oil into the surimi. The results indicated that the gel strength and hardness of bighead carp surimi increased significantly with higher oil substitution rates. When the myosin-κC Pickering emulsion completely replaced the oil, the gel hardness of surimi reached its highest level, and the L* value and whiteness significantly increased ( P < 0.05). Additionally, the water-holding capacity (WHC) of the surimi gel improved with increasing oil substitution rates. Myosin-κC Pickering emulsions were evenly distributed within the gel matrix as small oil droplets, filling the pores of the surimi and effectively enhancing the gel network structure. Sensory evaluation and gas phase ion migration spectrometry demonstrated that the myosin-κC Pickering emulsion improved sensory properties and reduced undesirable flavors when it completely replaced the oil. These results suggest that myosin-κC Pickering emulsion is beneficial for enhancing the properties and flavor of surimi gels.
研究领域:
食品科学
·
生物化学
✓ 已验证
产品关联
DOI
高影响因子
LWT-FOOD SCIENCE AND TECHNOLOGY
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2022
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IF 6.056
Wangli Dai,Wenjie Wang,Saiqi Gu,Mingjiang Xu,Hongzheng Yao,Xuxia Zhou,Yuting Ding
The effects of chitosan-epigallocatechin gallate (EGCG) coating on sensory properties and retention of volatile flavor compounds (VFCs) in chilled bighead carp fillets were examined. Scores of odor and overall acceptability indicated that as compared with the control group and group coated with chitosan, chitosan-EGCG coating had the best retention effect on the flavor and quality of the fillets. Twenty-eight VFCs, mainly alcohols, ketones, and aldehydes, were identified from the fillets by GC-IMS analysis. Fillets in the control group showed unique characteristic VFCs distribution at different storage stages: 2-butanone in the early stage; 3-methylbutanal and 2-methylbutanal in the middle stage; and heptanal and 1-octen-3-ol in the final stage. However, the VFCs signals in chitosan-EGCG coated fillets were delayed along with the sharply suppressed intensities of off-odor VFCs such as 1-octen-3-ol, indicating that chitosan-EGCG coating was able to inhibit the formation of off-odors effectively. Principal component analysis and clustering analysis distinguished samples with different storage times and treatments. This study indicated that chitosan-EGCG coating could maintain the flavor quality of bighead carp fillets, and the characteristic VFCs of different storage stages could be considered as signal indicators to identify fish freshness.
研究领域:
食品科学
·
生物化学
✓ 已验证
DOI
高影响因子
FOOD HYDROCOLLOIDS
·
2017
·
IF 4.747
Ruichang Gao,Yanmin Wang,Jianlou Mu,Tong Shi,Li Yuan
In this study, the effects of l -histidine (L-His) on the aggregation of bighead carp ( Aristichthys nobilis ) myosin induced by heating in low (0.1) or high (0.5) ionic strength solutions were studied. The solubility of natural myosin was significantly enhanced by L-His both in low and high ionic strength solutions. More small particles are suspended in the heated solution containing L-His, inducing a higher solubility than that solution without L-His. The surface hydrophobicity of myosin in a low ionic strength solution containing L-His is higher than that of myosin without L-His. The results of morphology show that L-His induced myosin to form finer aggregates and a honeycomb-like network in a low/high ionic strength solution during heat treatment. These results demonstrate that L-His might disrupt the electrostatic property of unfolded myosin heat-induced through electrostatic binding with the exposed negatively charged amino acid residues, which might disarrange hydrophobic surfaces, resulting in weakening hydrophobic interactions, which ultimately suppresses the fierce aggregation of carp myosin.
研究领域:
食品科学
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蛋白质化学
·
水产养殖
✓ 已验证
DOI
高影响因子
危险品化学品经营许可证（带存储）